Evidence map›Paper›PMID 32152681›Full record

ArticleEuropean biophysics journal : EBJ2020

NMR and crystallographic structural studies of the Elongation factor P from Staphylococcus aureus.

Alexander Golubev, Bulat Fatkhullin, Azat Gabdulkhakov, Aydar Bikmullin, Liliya Nurullina, Natalia Garaeva, Daut Islamov, Evelina Klochkova, Vladimir Klochkov, Albert Aganov and 5 more

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Article in European biophysics journal : EBJ, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.1field-weighted citation impact, top 57% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

4 citing papers in PubMed, 6 citations in OpenAlex.

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  2. Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

15 authors at 4 institutions in 3 countries.

Alexander GolubevLaboratory of Structural Biology, Institute of Fundamental Medicine and Biology, Kazan Federal University, 18 Kremlyovskaya, Kazan, 420008, Russian Federation.
Bulat FatkhullinLaboratory of Structural Biology, Institute of Fundamental Medicine and Biology, Kazan Federal University, 18 Kremlyovskaya, Kazan, 420008, Russian Federation.
Azat GabdulkhakovInstitute of Protein Research, Russian Academy of Sciences, Institutskaya 4, 142290, Puschino, Moscow Region, Russian Federation.
Aydar BikmullinLaboratory of Structural Biology, Institute of Fundamental Medicine and Biology, Kazan Federal University, 18 Kremlyovskaya, Kazan, 420008, Russian Federation.
Liliya NurullinaLaboratory of Structural Biology, Institute of Fundamental Medicine and Biology, Kazan Federal University, 18 Kremlyovskaya, Kazan, 420008, Russian Federation.
Natalia GaraevaLaboratory of Structural Biology, Institute of Fundamental Medicine and Biology, Kazan Federal University, 18 Kremlyovskaya, Kazan, 420008, Russian Federation.
Daut IslamovLaboratory of Structural Biology, Institute of Fundamental Medicine and Biology, Kazan Federal University, 18 Kremlyovskaya, Kazan, 420008, Russian Federation.
Evelina KlochkovaLaboratory of Structural Biology, Institute of Fundamental Medicine and Biology, Kazan Federal University, 18 Kremlyovskaya, Kazan, 420008, Russian Federation.
Vladimir KlochkovNMR Laboratory, Medical Physics Department, Institute of Physics, Kazan Federal University, 18 Kremlyovskaya, Kazan, 420008, Russian Federation.
Albert AganovNMR Laboratory, Medical Physics Department, Institute of Physics, Kazan Federal University, 18 Kremlyovskaya, Kazan, 420008, Russian Federation.
Iskander KhusainovLaboratory of Structural Biology, Institute of Fundamental Medicine and Biology, Kazan Federal University, 18 Kremlyovskaya, Kazan, 420008, Russian Federation.
Shamil ValidovLaboratory of Structural Biology, Institute of Fundamental Medicine and Biology, Kazan Federal University, 18 Kremlyovskaya, Kazan, 420008, Russian Federation.
Gulnara YusupovaDépartement de Biologie Et de Génomique Structurales, Institut de Génétique Et de Biologie Moléculaire Et Cellulaire, CNRS UMR7104, INSERM U964, Université de Strasbourg, 1 rue Laurent Fries, 67400, Illkirch, France.
Marat YusupovLaboratory of Structural Biology, Institute of Fundamental Medicine and Biology, Kazan Federal University, 18 Kremlyovskaya, Kazan, 420008, Russian Federation.
Konstantin UsachevLaboratory of Structural Biology, Institute of Fundamental Medicine and Biology, Kazan Federal University, 18 Kremlyovskaya, Kazan, 420008, Russian Federation. k.usachev@kpfu.ru.
Kazan Federal University · RUUniversité de Strasbourg · FRInstitute of Protein Research · RUCentre National de la Recherche Scientifique · FR

Funding

Russian Science Foundation 17-74-20009
6 · The paper itself

Abstract

Elongation factor P (EF-P) is a translation protein factor that plays an important role in specialized translation of consecutive proline amino acid motifs. EF-P is an essential protein for cell fitness in native environmental conditions. It regulates synthesis of proteins involved in bacterial motility, environmental adaptation and bacterial virulence, thus making EF-P a potential drug target. In the present study, we determined the solution and crystal structure of EF-P from the pathogenic bacteria Staphylococcus aureus at 1.48 Å resolution. The structure can serve as a platform for structure-based drug design of novel antibiotics to combat the growing antibiotic resistance of S. aureus.

Indexed as

Nuclear Magnetic Resonance, BiomolecularStaphylococcus aureusBacterial ProteinsCrystallography, X-RayModels, MolecularPeptide Elongation FactorsProtein DomainsBacterial Proteinsfactor EF-PPeptide Elongation FactorsDrug targetEF-PNMRProtein structureRibosomeStaphylococcus aureusX-ray

Identifiers

PMID32152681
OpenAlexW3010510913

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.